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Author (down) Wittenberger, James F.
Title Animal Social Behavior Type Book Whole
Year 1981 Publication Abbreviated Journal
Volume Issue Pages
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Corporate Author Thesis
Publisher Duxbury Press Place of Publication Boston Editor
Language Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN ISBN 978-0878722952 Medium
Area Expedition Conference
Notes Approved no
Call Number Equine Behaviour @ team @ Serial 4262
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Author (down) Waage Jk,
Title How the zebra got its stripes – biting flies as selective agents in the evolution of zebra coloration Type Journal Article
Year 1981 Publication Abbreviated Journal J ent Soc S Afr
Volume 44 Issue Pages 351-358
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Notes from Professor Hans Klingels Equine Reference List Approved no
Call Number Serial 1685
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Author (down) TURNER JR JW et al,
Title Elimination marking behavior in feral horses Type Journal Article
Year 1981 Publication Abbreviated Journal Can J Zool
Volume 59 Issue Pages 1561-1566
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Notes from Professor Hans Klingels Equine Reference List Approved no
Call Number Serial 1666
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Author (down) SchäFer M,
Title Beobachtungen zum interspezifischen Aggressionsverhalten eines Halbeselhybrid Type Journal Article
Year 1981 Publication Abbreviated Journal Säugetierk Mitt
Volume 29 Issue Pages 49-58
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Area Expedition Conference
Notes from Professor Hans Klingels Equine Reference List Approved no
Call Number Serial 1560
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Author (down) Saigo, S.
Title A transient spin-state change during alkaline isomerization of ferricytochrome c Type Journal Article
Year 1981 Publication Journal of Biochemistry Abbreviated Journal J Biochem (Tokyo)
Volume 89 Issue 6 Pages 1977-1980
Keywords Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry
Abstract Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH.
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Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0021-924X ISBN Medium
Area Expedition Conference
Notes PMID:6270075 Approved no
Call Number Equine Behaviour @ team @ Serial 3808
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Author (down) Saigo, S.
Title Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c Type Journal Article
Year 1981 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta
Volume 669 Issue 1 Pages 13-20
Keywords Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism
Abstract Equilibria and kinetics of alkaline isomerization of seven ferricytochromes c from vertebrates were studied by pH-titration and pH-jump methods in the pH region of 7-12. In the equilibrium behavior, no significant difference was detected among the cytochromes c, whereas marked differences in the kinetic behavior were observed. According to the kinetic behavior of the isomerization, the cytochromes c examined fall into three classes: Group I (horse, sheep, dog and pigeon cytochromes c), Group II (tuna and bonito cytochromes c) and Group III (rhesus monkey cytochrome c). The kinetic results are interpreted in terms of the sequential scheme: Neutral form in equilibrium with fast Transient form in equilibrium with slow Alkaline form where the neutral and alkaline forms are the species stable at neutral and alkaline pH, respectively, and the transient form is a kinetic intermediate. From comparison of the primary sequences of the seven cytochromes c and the classification of these cytochromes c, it is concluded that the amino acid substitution Phe/Tyr at the 46-th position has a major influence on the kinetic behavior. In Group II and III cytochromes c, the ionization of Tyr-46 is suggested to bring about loosening of the heme crevice and thus facilitate the ligand replacement involved in the isomerization.
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-3002 ISBN Medium
Area Expedition Conference
Notes PMID:6271238 Approved no
Call Number refbase @ user @ Serial 3871
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Author (down) Rubenstein Di,
Title Behavioural ecology of island feral horeses Type Journal Article
Year 1981 Publication Abbreviated Journal Equine. Vet. J.
Volume 13 Issue Pages 27-34
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Notes from Professor Hans Klingels Equine Reference List Approved no
Call Number Serial 1524
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Author (down) Roberts, J.; Hunter, M.L.; Kacelnik, A.
Title The ground effect and acoustic communication Type Journal Article
Year 1981 Publication Animal Behaviour. Abbreviated Journal Anim. Behav.
Volume 29 Issue 2 Pages 633-634
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Notes Approved no
Call Number Serial 2123
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Author (down) Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M.
Title Nature of the fast and slow refolding reactions of iron(III) cytochrome c Type Journal Article
Year 1981 Publication Biochemistry Abbreviated Journal Biochemistry
Volume 20 Issue 6 Pages 1622-1630
Keywords Animals; Ascorbic Acid; *Cytochrome c Group; Guanidines; Horses; Kinetics; Oxidation-Reduction; Protein Conformation; Spectrum Analysis
Abstract The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165--184), have been reinvestigated. The fast reaction has the major amplitude (78%) and is 100-fold faster than the slow reaction in these conditions (pH 7.2, 25 degrees C, 1.75 M guanidine hydrochloride). We show here that native cyt c is the product formed in the fast reaction as well as in the slow reaction. Two probes have been used to test for formation of native cyt c. absorbance in the 695-nm band and rate of reduction of by L-ascorbate. Different unfolded species (UF, US) give rise to the fast and slow refolding reactions, as shown both by refolding assays at different times after unfolding (“double-jump” experiments) and by the formation of native cyt c in each of the fast and slow refolding reactions. Thus the fast refolding reaction is UF leads to N and the slow refolding reaction is Us leads to N, where N is native cyt c, and there is a US in equilibrium UF equilibrium in unfolded cyt c. The results are consistent with the UF in equilibrium US reaction being proline isomerization, but this has not yet been tested in detail. Folding intermediates have been detected in both reactions. In the UF leads to N reaction, the Soret absorbance change precedes the recovery of the native 695-nm band spectrum, showing that Soret absorbance monitors the formation of a folding intermediate. In the US leads to N reaction an ascorbate-reducible intermediate has been found at an early stage in folding and the Soret absorbance change occurs together with the change at 695 nm as N is formed in the final stage of folding.
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Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-2960 ISBN Medium
Area Expedition Conference
Notes PMID:6261802 Approved no
Call Number Equine Behaviour @ team @ Serial 3809
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Author (down) Rau Re,
Title Zur Geschichte und Präparation der Mainzer Quaggas Type Journal Article
Year 1981 Publication Abbreviated Journal Mainzer Naturw Archiv
Volume 19 Issue Pages 221-236
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Notes from Professor Hans Klingels Equine Reference List Approved no
Call Number Serial 1498
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